Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2-hydroxypropyl-beta-cyclodextrin | HBC, solubilizes and activates | Rhodococcus erythropolis | |
2-hydroxypropyl-beta-cyclodextrin | HBC, solubilizes and activates. The addition of solubilizing agent causes AcmB to exhibit a higher affinity to cholest-4-en-3-one than to 4-androstene-3,17-dione | Sterolibacterium denitrificans |
Application | Comment | Organism |
---|---|---|
additional information | 3-oxosteroid DELAT1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications | Rhodococcus erythropolis |
additional information | 3-oxosteroid DELAT1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications | Sterolibacterium denitrificans |
Cloned (Comment) | Organism |
---|---|
gene amcB, recombinant enzyme expression in Escherichia coli | Sterolibacterium denitrificans |
gene kstD, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain XL10-Gold | Sterolibacterium denitrificans |
gene kstD1, recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Rhodococcus erythropolis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics, kinetic model | Rhodococcus erythropolis | |
additional information | - |
additional information | steady-state kinetics, kinetic model | Sterolibacterium denitrificans | |
0.0237 | - |
4-Cholesten-3-one | pH 6.5, 30°C, recombinant enzyme | Sterolibacterium denitrificans | |
0.0373 | - |
2,6-dichlorophenol-indophenol | pH 6.5, 30°C, recombinant enzyme, with 4-cholest-3-one | Sterolibacterium denitrificans | |
0.2235 | - |
2,6-dichlorophenol-indophenol | pH 6.5, 30°C, recombinant enzyme, with 4-androstene-3,17-dione | Sterolibacterium denitrificans | |
0.5292 | - |
4-androstene-3,17-dione | pH 6.5, 30°C, recombinant enzyme | Sterolibacterium denitrificans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | enzyme AcmB is located on the cytoplasmic side of the inner membranes of Sterolibacterium denitrificans | Sterolibacterium denitrificans | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-androstene-3,17-dione + acceptor | Rhodococcus erythropolis | - |
1,4-androstadiene-3,17-dione + reduced acceptor | - |
? | |
4-androstene-3,17-dione + acceptor | Sterolibacterium denitrificans | - |
1,4-androstadiene-3,17-dione + reduced acceptor | - |
? | |
4-cholesten-3-one + 2,6-dichlorophenol-indophenol | Sterolibacterium denitrificans | - |
? + reduced acceptor | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | Q9RA02 | - |
- |
Sterolibacterium denitrificans | A0A656Z7Q3 | - |
- |
Sterolibacterium denitrificans | A9XWD7 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli | Sterolibacterium denitrificans |
recombinant enzyme from Escherichia coli strain BL21(DE3) | Rhodococcus erythropolis |
recombinant enzyme from Escherichia coli strain XL10-Gold | Sterolibacterium denitrificans |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a 3-oxosteroid + acceptor = a 3-oxo-DELTA1-steroid + reduced acceptor | ping-pong bi bi mechanism | Sterolibacterium denitrificans | |
a 3-oxosteroid + acceptor = a 3-oxo-DELTA1-steroid + reduced acceptor | sequential linear mechanism | Rhodococcus erythropolis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-androstene-3,17-dione + acceptor | - |
Rhodococcus erythropolis | 1,4-androstadiene-3,17-dione + reduced acceptor | - |
? | |
4-androstene-3,17-dione + acceptor | - |
Sterolibacterium denitrificans | 1,4-androstadiene-3,17-dione + reduced acceptor | - |
? | |
4-androstene-3,17-dione + acceptor | KSTD1, which is reported to be inactive with this substrates can catalyze the reaction if the solubility problem is addressed, e.g. by 2-hydroxpropyl-beta-cyclodextrin | Rhodococcus erythropolis | 1,4-androstadiene-3,17-dione + reduced acceptor | - |
? | |
4-cholesten-3-one + 2,6-dichlorophenol-indophenol | - |
Rhodococcus erythropolis | ? + reduced acceptor | - |
? | |
4-cholesten-3-one + 2,6-dichlorophenol-indophenol | - |
Sterolibacterium denitrificans | ? + reduced acceptor | - |
? | |
6-dehydrotestosterone acetate + 2,6-dichlorophenol-indophenol | - |
Rhodococcus erythropolis | ? + reduced 2,6-dichlorophenol-indophenol | - |
? | |
6-dehydrotestosterone acetate + 2,6-dichlorophenol-indophenol | - |
Sterolibacterium denitrificans | ? + reduced 2,6-dichlorophenol-indophenol | - |
? | |
androstanolone + acceptor | - |
Rhodococcus erythropolis | ? + reduced acceptor | - |
? | |
androstanolone + acceptor | - |
Sterolibacterium denitrificans | ? + reduced acceptor | - |
? | |
diosgenone + acceptor | - |
Rhodococcus erythropolis | ? + reduced acceptor | - |
? | |
diosgenone + acceptor | - |
Sterolibacterium denitrificans | ? + reduced acceptor | - |
? | |
additional information | enzyme substrate specificity, structure-function analysis. Conversion of 4-androstene-3,17-dione and cholest-4-en-3-one by isozyme AcmB2 proceeds at a similar rate. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. AcmB2 shows ability to catalyze DELTA1-dehydrogenation of steroids with the aliphatic side chain on the C17 position | Sterolibacterium denitrificans | ? | - |
- |
|
additional information | enzyme substrate specificity, structure-function analysis. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. AcmB shows ability to catalyze DELTA1-dehydrogenation of steroids with the aliphatic side chain on the C17 position. AcmB indeed exhibits a significantly higher affinity to cholest-4-en-3-one than to 4-androstene-3,17-dione | Sterolibacterium denitrificans | ? | - |
- |
|
additional information | enzyme substrate specificity, structure-function analysis. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. Enzyme KSTD1 prefers smaller 3-oxosteroids | Rhodococcus erythropolis | ? | - |
- |
|
progesterone + 2,6-dichlorophenol-indophenol | - |
Rhodococcus erythropolis | pregna-1,4-diene-3,20-dione + reduced 2,6-dichlorophenol-indophenol | - |
? | |
progesterone + 2,6-dichlorophenol-indophenol | - |
Sterolibacterium denitrificans | pregna-1,4-diene-3,20-dione + reduced 2,6-dichlorophenol-indophenol | - |
? | |
testosterone propionate + 2,6-dichlorophenol-indophenol | - |
Rhodococcus erythropolis | 17beta-hydroxyandrost-1,4-diene-3-one propionate + reduced 2,6-dichlorophenol-indophenol | - |
? | |
testosterone propionate + 2,6-dichlorophenol-indophenol | - |
Sterolibacterium denitrificans | 17beta-hydroxyandrost-1,4-diene-3-one propionate + reduced 2,6-dichlorophenol-indophenol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-ketosteroid delta1-dehydrogenase | - |
Rhodococcus erythropolis |
3-ketosteroid delta1-dehydrogenase | - |
Sterolibacterium denitrificans |
AcmB | - |
Sterolibacterium denitrificans |
AcmB2 | - |
Sterolibacterium denitrificans |
cholest-4-en-3-one DELTA1-dehydrogenase | - |
Sterolibacterium denitrificans |
DELTA1-KstD | - |
Rhodococcus erythropolis |
DELTA1-KstD | - |
Sterolibacterium denitrificans |
KstD | - |
Sterolibacterium denitrificans |
KSTD1 | - |
Rhodococcus erythropolis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
- |
Rhodococcus erythropolis |
30 | - |
- |
Sterolibacterium denitrificans |
30 | - |
assay at | Sterolibacterium denitrificans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5.8 | - |
4-Cholesten-3-one | pH 6.5, 30°C, recombinant enzyme | Sterolibacterium denitrificans | |
46.1 | - |
4-androstene-3,17-dione | pH 6.5, 30°C, recombinant enzyme | Sterolibacterium denitrificans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Sterolibacterium denitrificans |
6.5 | - |
assay at | Sterolibacterium denitrificans |
8 | - |
- |
Rhodococcus erythropolis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
2,6-dichlorophenolindophenol | DCPIP | Rhodococcus erythropolis | |
2,6-dichlorophenolindophenol | DCPIP | Sterolibacterium denitrificans |
General Information | Comment | Organism |
---|---|---|
evolution | 3-oxosteroid DELTA1-dehydrogenases are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria | Rhodococcus erythropolis |
evolution | 3-oxosteroid DELTA1-dehydrogenases are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria | Sterolibacterium denitrificans |
additional information | three-dimensional structure of a 3-oxosteroid DELTA1-dehydrogenase and structure-function analysis, enzyme reaction mechanism analysis, overview | Sterolibacterium denitrificans |
additional information | three-dimensional structure of a 3-oxosteroid DELTA1-dehydrogenase and structure-function analysis, enzyme reaction mechanism analysis, overview. Molecular dynamics simulations on KSTD1 from Rhodococcus erythropolis | Rhodococcus erythropolis |
physiological function | 3-oxosteroid DELTA1-dehydrogenases (DELTA1-KSTDs) are FAD-dependent enzymes that catalyze the introduction of a double bond between the C1 and C2 atoms of the A-ring of 3-ketosteroid substrates. They play a critical role in the early steps of the degradation of the steroid core. Enzyme DELTA1-KSTD is also essential for steroid ring opening under anaerobic conditions | Rhodococcus erythropolis |
physiological function | 3-oxosteroid DELTA1-dehydrogenases (DELTA1-KSTDs) are FAD-dependent enzymes that catalyze the introduction of a double bond between the C1 and C2 atoms of the A-ring of 3-ketosteroid substrates. They play a critical role in the early steps of the degradation of the steroid core. Enzyme DELTA1-KSTD is also essential for steroid ring opening under anaerobic conditions | Sterolibacterium denitrificans |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
87.1 | - |
4-androstene-3,17-dione | pH 6.5, 30°C, recombinant enzyme | Sterolibacterium denitrificans |